AROC_VIBA7
ID AROC_VIBA7 Reviewed; 361 AA.
AC P39198; F7YND6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300};
DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; OrderedLocusNames=VAA_03439;
OS Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=882102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 68554 / 775;
RX PubMed=8021209; DOI=10.1128/jb.176.14.4226-4234.1994;
RA Chen Q., Actis L.A., Tolmasky M.E., Crosa J.H.;
RT "Chromosome-mediated 2,3-dihydroxybenzoic acid is a precursor in the
RT biosynthesis of the plasmid-mediated siderophore anguibactin in Vibrio
RT anguillarum.";
RL J. Bacteriol. 176:4226-4234(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 68554 / 775;
RX PubMed=21576332; DOI=10.1128/iai.05138-11;
RA Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., Crosa J.H.;
RT "Complete genome sequence of the marine fish pathogen Vibrio anguillarum
RT harboring the pJM1 virulence plasmid and genomic comparison with other
RT virulent strains of V. anguillarum and V. ordalii.";
RL Infect. Immun. 79:2889-2900(2011).
CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC yield chorismate, which is the branch point compound that serves as the
CC starting substrate for the three terminal pathways of aromatic amino
CC acid biosynthesis. This reaction introduces a second double bond into
CC the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21830.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEH32635.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L29562; AAA21830.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002284; AEH32635.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041945924.1; NC_015633.1.
DR AlphaFoldDB; P39198; -.
DR SMR; P39198; -.
DR EnsemblBacteria; AEH32635; AEH32635; VAA_03439.
DR KEGG; van:VAA_03439; -.
DR PATRIC; fig|882102.3.peg.1055; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_2_6; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000006800; Chromosome I.
DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 1.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; aroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..361
FT /note="Chorismate synthase"
FT /id="PRO_0000140671"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 125..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 238..239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 278
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 293..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT CONFLICT 54
FT /note="L -> R (in Ref. 1; AAA21830)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39145 MW; A12FA68507ADFADC CRC64;
MAGNSIGQHF RVMTFGESHG IALGCIVDGC PPGLEITEAD LQIDLDRRRP GTSLYTTQRR
EADEVKILSG VFEGKTTGTS IGLLIENTDQ RSTDYSDIKD KFRPGHADYT YHQKYGIRDY
RGGGRSSARE TAMRVAAGAI AKKYLKQEFG VEIRAYLSQM GDVCIDKVDW NEIENNAFFC
PDADKVAAFD QLIRDLKKEG DSIGAKIQVV ATNLPVGLGE PVFDRLDADI AHALMSINAV
KGVEIGDGFD VVQQKGSQHR DPLTPNGFRS NHAGGILGGI STGQDIVASI ALKPTSSITV
PGDTITRTGE PTQLITKGRH DPCVGIRAVP IAEAMLAIVL MDHLLRHRGQ NFAVQTETPK
I
